Summary for clan MD

Summary Alignment Structure Literature
Clan type peptidaseM15.001 - zinc D-Ala-D-Ala carboxypeptidase (Streptomyces-type) (Streptomyces albus), MEROPS Accession MER0001357 (peptidase unit: 116-255); PDB accession 1LBU
HistoryPEPTIDAS.TXT (SwissProt document)
DescriptionWater nucleophile; water bound by single zinc ion ligated to His, Asp and His
Contents of clanClan MD contains peptidases that are involved in bacterial cell wall biosynthesis and lysis.
EvidenceThe homology of families M15 and M74 is shown by similarities in the protein folds of zinc D-Ala-D-Ala carboxypeptidase (M15.001) and murein endopeptidase (M74.001).
Catalytic mechanismThe metal ligands occur in the motifs His-Xaa(6)-Asp and His-Xaa-His, which are characteristic of clan MD.
Peptidase activityTypes of peptidase activity include carboxypeptidase (subfamilies ##M15A##, ##M15B##), dipeptidase (##M15D##), and endopeptidase (##M15C##, M74).
Protein foldTertiary structures have been determined for members of families M15 (Bussiere et al., 1998) and M74 (Marcyjaniak et al., 2004). Peptidases in clan MD are alpha/beta proteins with a bundle of helices and a four strand beta sheet. Two of the zinc ligands are on the beta sheet.
Homologous non-peptidase familiesThe N-terminal effector domain of hedgehog protein has a similar fold (Hall et al., 1995).
Other databases SCOP55166


Family Family Type Peptidase Structure
M15 zinc D-Ala-D-Ala carboxypeptidase ({Streptomyces}-type) (Streptomyces albus) Yes
M74 murein endopeptidase (Escherichia coli) Yes

Distribution of clan MD among Kingdoms of Organisms